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姓名:和媛 性别:女 民族:汉
部门:有机化学与化学生物学学部
籍贯:陕西西安 职称:副教授
邮箱:yuanhe@nwu.edu.cn
研究方向: 化学糖生物学;酶催化反应机理;蛋白质晶体结构解析;小分子抑制剂开发;天然活性产物资源化;疾病快速检测;等温滴定微量热
简 介
2013-至今,西北大学化学与材料学院,副教授,第八批“陕西省百人”
2011-2013,加拿大 Simon Fraser University(David Vocadlo 教授实验室)/美国斯克利普斯研究所(The Scripps Research Institute; Jim Paulson 教授实验室)博士后
2007-2011,英国约克大学(the University of York) 博士 (化学)
2006-2007, 英国约克大学(the University of York) 硕士(功能基因组学专业)
2002-2006,西北大学理学学士
和媛副教授课题组主要从事疾病相关靶酶反应机理、高通量抑制剂筛选与设计、热力学表征、天然产物资源化等化学生物学研究。主要研究手段包括:X-射线晶体衍射、酶学、等温滴定微量热(ITC)、ELISA、流式细胞术、生物芯片等。研究成果发表在包括 JACS, Nature Structural & Molecular Biology, Nature Chemical Biology 等在内的著名国际期刊。该研究小组现招收化学生物学、有机化学、材料工程等相关专业的硕士研究生开展以下课题研究:
1.微量热技术用于酶活力表征的方法研究
2.病原微生物的化学糖生物学研究与药物开发
3.天然活性产物筛选
欢迎同学们来信咨询。
发表论文:
Wang,W.J., et al., Characterization of β-lactamase activity using isothermal titration calorimetry.BBA-General Gubjects, 2017. https://doi.org/10.1016/j.bbagen.2017.04.011
Macauley, M.S., et al., Unmasking of CD22 Co-receptor on Germinal Center B-cells Occurs by Alternative Mechanisms in Mouse and Man. J Biol Chem, 2015. 290(50): 30066-77.
He, Y., et al., Three-dimensional structure of a Streptomyces sviceus GNAT acetyltransferase with similarity to the C-terminal domain of the human GH84 O-GlcNAcase. Acta Crystallogr D, 2014. 70: 186-95.
Rillahan, C.D., et al., Disubstituted Sialic Acid Ligands Targeting Siglecs CD33 and CD22 Associated with Myeloid Leukaemias and B Cell Lymphomas. Chem Sci, 2014. 5(6): 2398-2406.
Darby, J.F., et al., Discovery of selective small-molecule activators of a bacterial glycoside hydrolase. Angew Chem Int Ed, 2014. 53(49): 13419-23.
Macauley, M.S., et al., Metabolism of vertebrate amino sugars with N-glycolyl groups: intracellular beta-O-linked N-glycolylglucosamine (GlcNGc), UDP-GlcNGc, and the biochemical and structural rationale for the substrate tolerance of beta-O-linked beta-N-acetylglucosaminidase. J Biol Chem, 2012. 287(34): 28882-97.
He, Y., et al., Inhibition of a bacterial O-GlcNAcase homologue by lactone and lactam derivatives: structural, kinetic and thermodynamic analyses. Amino Acids, 2011. 40(3): 829-39.
Macauley, M.S., et al., Inhibition of O-GlcNAcase using a potent and cell-permeable inhibitor does not induce insulin resistance in 3T3-L1 adipocytes. Chem Biol, 2010. 17(9): 937-48.
Martinez-Fleites, C., Y. He, and G.J. Davies, Structural analyses of enzymes involved in the O-GlcNAc modification. Biochim Biophys Acta, 2010. 1800(2): 122-33.
He, Y., et al., Visualizing the reaction coordinate of an O-GlcNAc hydrolase. J Am Chem Soc, 2010. 132(6): 1807-9.
He, Y., et al., Structural insight into the mechanism of streptozotocin inhibition of O-GlcNAcase. Carbohydr Res, 2009. 344(5): 627-31.
Marcelo, F., et al., Molecular basis for inhibition of GH84 glycoside hydrolases by substituted azepanes: conformational flexibility enables probing of substrate distortion. J Am Chem Soc, 2009. 131(15): 5390-2.
Balcewich, M.D., et al., Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ. Protein Sci, 2009. 18(7): 1541-51.
Martinez-Fleites, C., et al., Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nat Struct Mol Biol, 2008. 15(7): 764-5.
Yuzwa, S.A., et al., A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo. Nat Chem Biol, 2008. 4(8): 483-90.
Wang, Z.F., Y. He, and L.J. Huang, An alternative method for the rapid synthesis of partially O-methylated alditol acetate standards for GC-MS analysis of carbohydrates. Carbohydr Res, 2007. 342(14): 2149-51.
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